L-lactate oxidase
| L-lactate oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.3.2 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
L-lactate oxidase (EC 1.1.3.2) is an enzyme that catalyzes the chemical reaction:[1][2][3]
It belongs to the family of oxidoreductases (enzymes involved in redox reactions), specifically those acting on the CH−OH group of donors with oxygen as acceptor. The systematic name of this enzyme class is (S)-lactate:oxygen 2-oxidoreductase. It employs one cofactor, flavin mononucleotide.[4] The amino acid sequence of this enzyme is similar to that in lactate 2-monooxygenase, which converts lactate to acetate and carbon dioxide. The difference in the products formed has been ascribed to differences in the stability of an intermediate complex.[3]
The enzyme was first isolated and characterised from the bacterium Aerococcus viridans.[2] The relevant genes from Streptococcus iniae were subsequently cloned to allow further study.[5] These developments have allowed the enzyme to be used in biosensors which measure the concentration of lactic acid in blood.[1][6][7]
Structural studies
Tertiary structures have been solved for this class of enzymes,[8] with the PDB accession code PDB: 2DU2.[9]
References
- 1 2 Enzyme 1.1.3.2 at KEGG Pathway Database.
- 1 2 Duncan, John D.; Wallis, John O.; Azari, Mahmood R. (1989). "Purification and properties of Aerococcus viridans lactate oxidase". Biochemical and Biophysical Research Communications. 164 (2): 919–926. doi:10.1016/0006-291X(89)91546-5. PMID 2818595.
- 1 2 Maeda-Yorita, K.; Aki, K.; Sagai, H.; Misaki, H.; Massey, V. (1995). "L-lactate oxidase and L-lactate monooxygenase: Mechanistic variations on a common structural theme". Biochimie. 77 (7–8): 631–642. doi:10.1016/0300-9084(96)88178-8. PMID 8589073.
- ↑ Stoisser, Thomas; Brunsteiner, Michael; Wilson, David K.; Nidetzky, Bernd (2016). "Conformational flexibility related to enzyme activity: Evidence for a dynamic active-site gatekeeper function of Tyr215 in Aerococcus viridans lactate oxidase". Scientific Reports. 6 27892. doi:10.1038/srep27892. PMC 4908395. PMID 27302031.
- ↑ Gibello, A.; Collins, M. D.; DomíNguez, L.; FernáNdez-GarayzáBal, J. F.; Richardson, P. T. (1999). "Cloning and Analysis of the l -Lactate Utilization Genes from Streptococcus iniae". Applied and Environmental Microbiology. 65 (10): 4346–4350. doi:10.1128/AEM.65.10.4346-4350.1999. PMC 91576. PMID 10508058.
- ↑ Arduini, Fabiana; Amine, Aziz (2013). "Biosensors Based on Enzyme Inhibition". Biosensors Based on Aptamers and Enzymes. Advances in Biochemical Engineering/Biotechnology. Vol. 140. pp. 299–326. doi:10.1007/10_2013_224. ISBN 978-3-642-54142-1. PMID 23934362.
- ↑ Pagán, Miraida; Suazo, Dámaris; Del Toro, Nicole; Griebenow, Kai (2015). "A comparative study of different protein immobilization methods for the construction of an efficient nano-structured lactate oxidase-SWCNT-biosensor". Biosensors and Bioelectronics. 64: 138–146. doi:10.1016/j.bios.2014.08.072. PMC 4254293. PMID 25216450.
- ↑ Furuichi, Makio; Suzuki, Nobuhiro; Dhakshnamoorhty, Balasundaresan; et al. (2008). "X-ray Structures of Aerococcus viridans Lactate Oxidase and Its Complex with d-Lactate at pH 4.5 Show an α-Hydroxyacid Oxidation Mechanism". Journal of Molecular Biology. 378 (2): 436–446. doi:10.1016/j.jmb.2008.02.062. PMID 18367206.
- ↑ Umena, Yasufumi; Yorita, Kazuko; Matsuoka, Takeshi; Kita, Akiko; Fukui, Kiyoshi; Morimoto, Yukio (2006). "The crystal structure of l-lactate oxidase from Aerococcus viridans at 2.1 Å resolution reveals the mechanism of strict substrate recognition". Biochemical and Biophysical Research Communications. 350 (2): 249–256. doi:10.1016/j.bbrc.2006.09.025. PMID 17007814.